Crystal structure of human PNP complexed with hypoxanthine and sulfate ion

Canduri, Fernanda; Fadel, Valmir; Dias, Marcio Vinícius Bertacine; Basso, Luiz Augusto; Palma, Mário Sérgio; Santos, Diógenes Santiago; Azevedo Júnior, Walter Filgueira de

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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Crystal structure of human PNP complexed with hypoxanthine and sulfate ion

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Author(s):	Canduri, Fernanda ; Fadel, Valmir ; Dias, Marcio Vinícius Bertacine ^[3] ; Basso, Luiz Augusto ; Palma, Mário Sérgio ; Santos, Diógenes Santiago ; Azevedo Júnior, Walter Filgueira de Total Authors: 7
Document type:	Journal article
Source:	Biochemical and Biophysical Research Communications; v. 326, n. 2, p. 335-338, Jan. 2005.
Field of knowledge:	Biological Sciences - Biophysics
Abstract
Purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme, which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effects on B-cell function. Human PNP has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Here we report the crystal structure of human PNP in complex with hypoxanthine, refined to 2.6 resolution. The intermolecular interaction between ligand and PNP is discussed. (AU)

FAPESP's process:	01/07532-0 - Structural genomics of cyclin dependent kinases and plant defensive proteinases and their natural inhibitors
Grantee:	Walter Filgueira de Azevedo Junior
Support Opportunities:	Regular Research Grants

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